Evidence map›Paper›PMID 38494075›Full record

ReviewThe Journal of biological chemistry2024

Exploring the IRE1 interactome: From canonical signaling functions to unexpected roles.

Simon Le Goupil, Hadrien Laprade, Marc Aubry, Eric Chevet

Open access · goldAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
11.4field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

30 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Functional Characterization of a Signal Peptide Peptidase inInternational journal of molecular sciences · 2026
    Article
  10. Review
  11. The "cutting edge" of non-canonical RNA splicing.Frontiers in molecular biosciences · 2026
    Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Molecular Basis of Intron Retention inInternational journal of molecular sciences · 2025
    Article
  18. Article
  19. Article
  20. Mitochondria-Nuclear Crosstalk: Orchestrating mtDNA Maintenance.Environmental and molecular mutagenesis · 2025
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Simon Le GoupilINSERM U1242, University of Rennes, Rennes, France; Centre de Lutte contre le cancer Eugène Marquis, Rennes, France. Electronic address: simon.legoupil@univ-rennes1.fr.
Hadrien LapradeINSERM U1242, University of Rennes, Rennes, France; Centre de Lutte contre le cancer Eugène Marquis, Rennes, France.
Marc AubryINSERM U1242, University of Rennes, Rennes, France; Centre de Lutte contre le cancer Eugène Marquis, Rennes, France.
Eric ChevetINSERM U1242, University of Rennes, Rennes, France; Centre de Lutte contre le cancer Eugène Marquis, Rennes, France.
Inserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The unfolded protein response is a mechanism aiming at restoring endoplasmic reticulum (ER) homeostasis and is likely involved in other adaptive pathways. The unfolded protein response is transduced by three proteins acting as sensors and triggering downstream signaling pathways. Among them, inositol-requiring enzyme 1 alpha (IRE1α) (referred to as IRE1 hereafter), an endoplasmic reticulum-resident type I transmembrane protein, exerts its function through both kinase and endoribonuclease activities, resulting in both X-box binding protein 1 mRNA splicing and RNA degradation (regulated ire1 dependent decay). An increasing number of studies have reported protein-protein interactions as regulators of these signaling mechanisms, and additionally, driving other noncanonical functions. In this review, we deliver evolutive and structural insights on IRE1 and further describe how this protein interaction network (interactome) regulates IRE1 signaling abilities or mediates other cellular processes through catalytic-independent mechanisms. Moreover, we focus on newly discovered targets of IRE1 kinase activity and discuss potentially novel IRE1 functions based on the nature of the interactome, thereby identifying new fields to explore regarding this protein's biological roles.

Indexed as

EndoribonucleasesProtein Interaction MapsProtein Serine-Threonine KinasesSignal TransductionAnimalsEndoplasmic ReticulumEvolution, MolecularHumansUnfolded Protein ResponseEndoribonucleasesERN1 protein, humanProtein Serine-Threonine Kinasesendoplasmic reticuluminteractomeIRE1protein homeostasissignalingstressunfolded protein response

Identifiers

PMID38494075
PMCPMC11007444
OpenAlexW4392844910

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.